Ricard-Blum Sylvie, Ruggiero Florence
Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS UCBL, IFR128 Biosciences Gerland, Lyon, France.
Pathol Biol (Paris). 2005 Sep;53(7):430-42. doi: 10.1016/j.patbio.2004.12.024. Epub 2005 Jan 20.
The collagen superfamily is highly complex and shows a remarkable diversity in molecular and supramolecular organization, tissue distribution and function. However, all its members share a common structural feature, the presence of at least one triple-helical domain, which corresponds to a number of (Gly-X-Y)n repeats (X being frequently proline and Y hydroxyproline) in the amino acid sequence. Several sub-families have been determined according to sequence homologies and to similarities in the structural organization and supramolecular assembly. In the present review, we focus on the newly described fibrillar collagens, fibrillar-associated collagens with interrupted triple helix, membrane collagens and multiplexins. Recent advances in the characterization of proteins containing triple-helical domains but not referred to as collagens are also discussed.
胶原超家族高度复杂，在分子和超分子组织、组织分布及功能方面表现出显著的多样性。然而，其所有成员都具有一个共同的结构特征，即至少存在一个三螺旋结构域，该结构域在氨基酸序列中对应多个(Gly-X-Y)n重复序列（X通常为脯氨酸，Y为羟脯氨酸）。根据序列同源性以及结构组织和超分子组装的相似性，已确定了几个亚家族。在本综述中，我们重点关注新描述的纤维状胶原、具有中断三螺旋的纤维状相关胶原、膜性胶原和多重胶原。还讨论了含有三螺旋结构域但未被称为胶原的蛋白质表征方面的最新进展。
